ID ARAA_ECOUT Reviewed; 500 AA. AC Q1RGD7; DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 16-MAY-2006, sequence version 1. DT 16-JUN-2009, entry version 21. DE RecName: Full=L-arabinose isomerase; DE EC=5.3.1.4; GN Name=araA; OrderedLocusNames=UTI89_C0067; OS Escherichia coli (strain UTI89 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=364106; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16585510; DOI=10.1073/pnas.0600938103; RA Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., RA Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., RA Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., RA Hultgren S.J., Gordon J.I.; RT "Identification of genes subject to positive selection in RT uropathogenic strains of Escherichia coli: a comparative genomics RT approach."; RL Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006). CC -!- FUNCTION: Catalyzes the conversion of L-arabinose to L-ribulose CC (By similarity). CC -!- CATALYTIC ACTIVITY: L-arabinose = L-ribulose. CC -!- COFACTOR: Binds 1 manganese ion per subunit (By similarity). CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L- CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacteria CC route): step 1/3. CC -!- SUBUNIT: Homohexamer (By similarity). CC -!- SIMILARITY: Belongs to the arabinose isomerase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CP000243; ABE05577.1; -; Genomic_DNA. DR RefSeq; YP_539108.1; -. DR SMR; Q1RGD7; 1-498. DR GeneID; 3993628; -. DR GenomeReviews; CP000243_GR; UTI89_C0067. DR KEGG; eci:UTI89_C0067; -. DR HOGENOM; Q1RGD7; -. DR OMA; Q1RGD7; EVCPTIA. DR BioCyc; ECOL364106:UTI89_C0067-MON; -. DR GO; GO:0008733; F:L-arabinose isomerase activity; IEA:HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-KW. DR GO; GO:0019568; P:arabinose catabolic process; IEA:HAMAP. DR HAMAP; MF_00519; -; 1. DR InterPro; IPR003762; Lara_isomerase. DR Pfam; PF02610; Arabinose_Isome; 1. DR PIRSF; PIRSF001478; L-ara_isomerase; 1. DR ProDom; PD018364; Lara_isomerase; 1. PE 3: Inferred from homology; KW Arabinose catabolism; Carbohydrate metabolism; Complete proteome; KW Isomerase; Manganese; Metal-binding. FT CHAIN 1 500 L-arabinose isomerase. FT /FTId=PRO_0000259337. FT METAL 306 306 Manganese (By similarity). FT METAL 333 333 Manganese (By similarity). FT METAL 350 350 Manganese (By similarity). FT METAL 450 450 Manganese (By similarity). SQ SEQUENCE 500 AA; 56103 MW; E1B1B9F2FACF1FBD CRC64; MTIFDNYEVW FVIGSQHLYG PETLRQVTQH AEHVVNALNT EAKLPCKLVL KPLGTTPDEI TAICRDANYD DRCAGLVVWL HTFSPAKMWI NGLTMLNKPL LQFHTQFNAA LPWDSIDMDF MNLNQTAHGG REFGFIGARM RQQHAVVTGH WQDKQAHERI GSWMRQAVSK QDTRHLKVCR FGDNMREVAV TDGDKVAAQI KFGFSVNTWA VGDLVQVVNS ISDGDVNALV DEYESCYTMT PATQIHGEKR QNVLEAARIE LGMKRFLEQG GFHAFTTTFE DLHGLKQLPG LAVQRLMQQG YGFAGEGDWK TAALLRIMKV MSTGLQGGTS FMEDYTYHFE KGNDLVLGSH MLEVCPSIAV EEKPILDVQH LGIGGKDDPA RLIFNTQTGP AIVASLIDLG DRYRLLVNCI DTVKTPHSLP KLPVANALWK AQPDLPTASE AWILAGGAHH TVFSHALNLN DMRQFAEMHD IEITVIDNDT RLPAFKDALR WNEVYYGFRR //